Characterization of a Crosslinked Elastomeric‐Protein Inspired Polypeptide

Abstract

Materials inspired by natural proteins have a great appeal in tissue engineering for their biocompatibility and similarity to extracellular matrix (ECM). Chimeric polypeptides inspired by elastomeric proteins such as silk, elastin, and collagen are of outstanding interest in the field. A recombinant polypeptide constituted of three different blocks, each of them having sequences derived from elastin, resilin, and collagen proteins, was demonstrated to be a good candidate as biomaterial for its self-assembling characteristics and biocompatibility. Herein, taking advantage of the primary amine functionalities present in the linear polypeptide, we crosslinked it with 1,6-hexamethylene-diisocyanate (HMDI). The characterization of the obtained polypeptide was realized by CD spectroscopy, AFM, and SEM microscopies. The obtained results, although not conclusive, demonstrate that the crosslinked polypeptide gave rise to porous networks, thin nanowires, and films not observable for the linear polypeptide. Chirality 28:606-611, 2016. © 2016 Wiley Periodicals, Inc.

Soft Hydrogel Inspired by Elastomeric Proteins

“…An electrophoretic mobility delay that determines an apparently higher molecular weight has been previously described in recombinant protein polymers whose composition in hydrophobic amino acids was around 80%, the same percentage of REC biopolymers. 15 Finally, due to the good expression yield of (REC) 3 , its gene was subcloned in another modified pET expression vector (pET 14 H8) ( Figures S1B and S4 ) to insert an octahistidine tag that allows its purification by IMAC. The obtained (REC) 3 polypeptide is a 442-amino-acid polymer whose complete sequence is shown in Figure S6 .…”

“… 14 Accordingly, glycine-rich polypeptides are emerging as an alternative class of elastin-inspired polypeptides in the design of recombinantly expressed polypeptides for biomedical applications. 15 − 18 Recombinant elastomeric polypeptides were commonly enriched with adhesion sequences in order to improve cell invasion and spreading; however, adhesion to tissues could be detrimental in clinical practice, causing severe pain and inflammation as postsurgery complications. 19 Several biomaterials, such as polyethylene glycol, were developed as active methods to prevent postsurgery adhesion, working mainly as a physical barrier.…”

Fibrillar Self-Assembly of a Chimeric Elastin-Resilin Inspired Engineered Polypeptide

“…The chimera is a mythical hybrid monster composed of the parts of more than one animal: a lion with the tail of a snake and the head of a goat. Analogously, the chimera could be made of different proteins, such as elastin, resilin, and collagen (REC)-inspired sequences [1]. REC exhibited tunable self-assembling and a quasi-ideal elastomeric behavior [2].…”

Photoinduced Thiol‐ene Chemistry Applied to the Synthesis of Self‐Assembling Elastin‐Inspired Glycopeptides

“…All of them are present in the form of fibers considered crucial for the exerted biological role . Elastin is widely considered as an inspiring protein for the design of biomaterials due to its poor immunogenicity and high biocompatibility . Furthermore, elastin is characterized by repetitive motifs thoroughly repeated along the primary structure and considered significant for its function.…”

“…[1] Elastin is widely considered as an inspiringp rotein for the design of biomaterialsd ue to its poor immunogenicity andh igh biocompatibility. [2] Furthermore, elastin is characterizedb yr epetitive motifs thoroughlyr epeated along the primary structure and considered significant for its function. Short elastin-inspired peptides constituted of these repetitive motifs are an interesting class of self-assembling materials able to give rise to fibrilsd espite of their small size.…”